The crystal structure of an uncharacterized domain of P113 from Plasmodium falciparum

P113 is a membrane-anchored protein in Plasmodium falciparum that stabilizes the RH5 complex, facilitating erythrocyte invasion by interacting with the host receptor basigin. The helical-rich domain of P113 (residues 311–679) was crystallized, revealing a predominantly α-helical structure with two four-helix bundles and a disordered connecting region.

Structure of the Fab fragment of a humanized 5E5 antibody to a cancer-specific Tn-MUC1 epitope

The structure of the humanized Fab from murine monoclonal antibody 5E5 specific for tumor antigen Tn-MUC1 has been determined to 1.57 Å resolution. The humanization process has imposed changes in the framework regions of the Fv which may have affected the Vh–Vl interface.

Structures of α-galactosaminidases from the CAZy GH114 family and homologs defining a new GH191 family of glycosidases

Structural and functional analysis of a new fungal GH114 endo-α-1,4-galactosaminidase, along with homologs that establish a new GH191 family of glycoside hydrolases, are reported. In addition, various crystal pathologies led to the development of a new refinement procedure for disordered structures.

Unique double-helical packing of protein molecules in the crystal of potassium-independent L-asparaginase from common bean

The crystal structure of the potassium-independent L-asparaginase PvAIII, with a rare P2 space-group symmetry, shows an unusual pseudosymmetric 4₁-like double-helical packing with 32 protein chains in the asymmetric unit. The packing is determined by an extended intermolecular β-sheet, by incomplete degradation of the interdomain linker. and by intermolecular `hydrogen-bond linchpins' that connect adjacent protein chains together.

Robust error calibration for serial crystallography

We present a new error-calibration algorithm for reflection intensities in serial crystallography. We reformulate the mathematical basis of the problem and apply different levels of uncertainty to each observed lattice corresponding to its measurement accuracy. These uncertainties are more consistent with theoretical expectations than the Ev11 error-calibration algorithm previously implemented in cctbx.xfel.merge.